help button home button
AJRCMB
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Muimo, R.
Right arrow Articles by Mehta, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Muimo, R.
Right arrow Articles by Mehta, A.

Am. J. Respir. Cell Mol. Biol., Volume 18, Number 2, February, 1998 270-278

Nucleoside Diphosphate Kinase and Clminus -sensitive Protein Phosphorylation in Apical Membranes from Ovine Airway Epithelium

Richmond Muimo, Stephen J. Banner, Lindsay J. Marshall, and Anil Mehta

Department of Child Health, Centre for Research into Human Development, Ninewells Hospital Medical School, Dundee, Scotland, United Kingdom

We have previously shown that nucleotide species (adenosine triphosphate [ATP] or guanosine triphosphate [GTP]), [Cl-], and anion species determine the steady-state phosphorylation of apical membrane proteins within human airway epithelium in vitro. We found that a Cl--regulated 37-kD protein (p37) principally phosphorylated with GTP but not ATP as substrate. Here we show that apical membranes from sheep tracheal epithelium also contain a Cl--regulated 37-kD phosphoprotein (p37s) and characterize one of the kinases involved in the regulation of p37s. Analysis of phosphorylation of apical membrane proteins with gamma [32P]GTP in the presence of MgCl2 showed that two proteins circa 19 and 21 kD (p19s and p21s) were transiently phosphorylated before p37s. Renaturation of apical membrane proteins within polyacrylamide gels showed that p19s and p21s autophosphorylated with either gamma [32P]GTP or gamma [32P]ATP as substrates, suggesting that the two proteins were kinases. Immunoblotting and immunoprecipitation with a specific polyclonal antibody showed that p21s was a membrane-bound isoform of nucleoside diphosphate kinase (NDPK, EC 2.7.4.6), a protein kinase which catalyzes transfer of terminal phosphate from ATP to diphosphate nucleotides and is, among other functions, essential for cell secretion. Incubation of apical membrane proteins in the presence of gamma [32P]ATP and guanosine diphosphate (GDP) (but not GDPbeta S) resulted in enhancement of phosphorylation of p37s. Dephosphorylation of NDPK was stimulated by the addition of Mg2+, Mn2+, and Co2+ (but not Zn2+ or Ca2+). Our data show that ovine trachea is a good model for further characterization of the chloride-dependent cascade in airway epithelium.




This article has been cited by other articles:


Home page
 Exp PhysiolHome page
K. J Treharne, R. M Crawford, and A Mehta
CFTR, chloride concentration and cell volume: could mammalian protein histidine phosphorylation play a latent role?
Exp Physiol, January 1, 2006; 91(1): 131 - 139.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
P. Van Damme, G. Callewaert, J. Eggermont, W. Robberecht, and L. Van Den Bosch
Chloride Influx Aggravates Ca2+-Dependent AMPA Receptor-Mediated Motoneuron Death
J. Neurosci., June 15, 2003; 23(12): 4942 - 4950.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Cuello, R. A. Schulze, F. Heemeyer, H. E. Meyer, S. Lutz, K. H. Jakobs, F. Niroomand, and T. Wieland
Activation of Heterotrimeric G Proteins by a High Energy Phosphate Transfer via Nucleoside Diphosphate Kinase (NDPK) B and Gbeta Subunits. COMPLEX FORMATION OF NDPK B WITH Gbeta gamma DIMERS AND PHOSPHORYLATION OF His-266 IN Gbeta
J. Biol. Chem., February 21, 2003; 278(9): 7220 - 7226.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
L. J. Marshall, R. Muimo, C. E. Riemen, and A. Mehta
Na+ and K+ regulate the phosphorylation state of nucleoside diphosphate kinase in human airway epithelium
Am J Physiol Cell Physiol, January 1, 1999; 276(1): C109 - C119.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Muimo, Z. Hornickova, C. E. Riemen, V. Gerke, H. Matthews, and A. Mehta
Histidine Phosphorylation of Annexin I in Airway Epithelia
J. Biol. Chem., November 17, 2000; 275(47): 36632 - 36636.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Proc. Am. Thorac. Soc. Am. J. Respir. Crit. Care Med.
Copyright © 1998 American Thoracic Society.